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The greatest enzyme yield was attained when the submerged fermentation (SmF) conditions were optimized, and it was around (39.7\u00a0U\/mg protein). Moreover, upon optimization of fibrinolytic enzyme production under solid\u2010state fermentation (SSF), the maximum productivity of fibrinolytic enzyme was greatly increased recorded a bout (405\u00a0U\/mg protein) on sugarcane bagasse, incubation period of 5 days, moisture level of 100%, initial pH of salt basal medium 7.8, incubation temperature at 35\u00b0C, and supplementation of the salt basal medium with corn steep liquor (80\uff05, v\/v). The yield of fibrinolytic enzyme by <jats:italic>C. hawaiiensis<\/jats:italic> under SSF was higher than that of SmF with about 10.20\u2010fold. The purification procedures of fibrinolytic enzyme by ammonium sulfate (70%), gel filtration, and ion\u2010exchange columns chromatography caused a great increase in its specific activity to 2581.6\u00a0U\/mg protein with an overall yield of 55.89%, 6.37 purification fold and molecular weight of 35\u00a0kDa. Maximal activity was recorded at pH 7 and 37\u00b0C. Significant pH stability was recorded at pH 6.6\u20137.2, and thermal stability was recorded at 33\u201341\u00b0C. The enzyme showed the highest affinity toward fibrin, with <jats:italic>V<\/jats:italic><jats:sub>max<\/jats:sub> of 240\u00a0U\/mL and an apparent Km value of 47.61\u00a0mmol. Mg<jats:sup>2+<\/jats:sup> and Ca<jats:sup>2+<\/jats:sup> moderately induced fibrinolytic activity, whereas Cu<jats:sup>2+<\/jats:sup> and Zn<jats:sup>2+<\/jats:sup> greatly suppressed the enzyme activity. The produced enzyme is categorized as serine protease and non\u2010metalloprotease. The purified fibrinolytic enzyme showed efficient thrombolytic and antiplatelet aggregation activities by completely prevention and dissolution of the blood clot which confirmed by microscopic examination and amelioration of blood coagulation assays. These findings suggested that the produced fibrinolytic enzyme is a promising agent in management of blood coagulation disorders.<\/jats:p>","DOI":"10.1002\/bab.2502","type":"journal-article","created":{"date-parts":[[2023,7,19]],"date-time":"2023-07-19T02:28:46Z","timestamp":1689733726000},"page":"1954-1971","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Thrombolytic and anticoagulant efficiencies of purified fibrinolytic enzyme produced from <i>Cochliobolus hawaiiensis<\/i> under solid\u2010state fermentation"],"prefix":"10.1002","volume":"70","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2215-3660","authenticated-orcid":false,"given":"Medhat Ahmed","family":"Abu\u2010Tahon","sequence":"first","affiliation":[{"name":"Department of Biology, Faculty of Science and Arts Northern Border University Rafha Saudi Arabia"},{"name":"Biological and Geological Sciences Department, Faculty of Education Ain Shams 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